Detail Information for IndEnz0016000022
IED ID IndEnz0016000022
Enzyme Type ID tyrosinase000022
Protein Name Tyrosinase
EC 1.14.18.1
Monophenol monooxygenase
Gene Name TYR
Organism Bos taurus (Bovine)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Metazoa Eumetazoa Bilateria Deuterostomia Chordata Craniata Vertebrata Gnathostomata (jawed vertebrates) Teleostomi Euteleostomi Sarcopterygii Dipnotetrapodomorpha Tetrapoda Amniota Mammalia Theria Eutheria Boreoeutheria Laurasiatheria Artiodactyla Ruminantia Pecora Bovidae Bovinae Bos (oxen cattle) Bos taurus (Bovine)
Enzyme Sequence MLLAALYCLLWSFRTSAGHFPRACASSKSLTEKECCPPWAGDGSPCGRLSGRGSCQDVILSTAPLGPQFPFTGVDDRESWPSIFYNRTCQCFSNFMGFNCGSCKFGFRGPRCTERRLLVRRNIFDLSVPEKNKFLAYLTLAKHTTSPDYVIPTGTYGQMNHGTTPLFNDVSVYDLFVWMHYYVSRDTLLGDSEVWRDIDFAHEAPGFLPWHRLFLLLWEQEIQKLTGDENFTIPYWDWRDAENCDVCTDEYMGGRNPANPNLLSPASFFSSWQIVCSRLEEYNSRQALCNGTSEGPLLRNPGNHDKARTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFADPVTGIADASQSSMHNALHIYMNGTMSQVPGSANDPIFLLHHAFVDSIFEQWLRKYHPLQDVYPEANAPIGHNRESYMVPFIPLYRNGDFFISSKDXGYDYSYLQDSEPDIFQDYIKPYLEQAQRIWPWLIGAAVVGSVLTAVLGGLTSLLCRRKRNQLPEEKQPLLMEKEDYHNLMYQSHL
Enzyme Length 530
Uniprot Accession Number Q8MIU0
Absorption
Active Site
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=2 L-dopa + O2 = 2 H2O + 2 L-dopaquinone; Xref=Rhea:RHEA:34287, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57504, ChEBI:CHEBI:57924; EC=1.14.18.1; Evidence={ECO:0000250|UniProtKB:P11344}; CATALYTIC ACTIVITY: Reaction=L-tyrosine + O2 = H2O + L-dopaquinone; Xref=Rhea:RHEA:18117, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:57924, ChEBI:CHEBI:58315; EC=1.14.18.1; Evidence={ECO:0000250|UniProtKB:P11344};
DNA Binding
EC Number 1.14.18.1
Enzyme Function FUNCTION: This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds (By similarity). Catalyzes the initial and rate limiting step in the cascade of reactions leading to melanin production from tyrosine (By similarity). In addition to hydroxylating tyrosine to DOPA (3,4-dihydroxyphenylalanine), also catalyzes the oxidation of DOPA to DOPA-quinone, and possibly the oxidation of DHI (5,6-dihydroxyindole) to indole-5,6 quinone (By similarity). {ECO:0000250|UniProtKB:P11344}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Chain (1); Glycosylation (5); Metal binding (6); Sequence conflict (1); Signal peptide (1); Topological domain (2); Transmembrane (1)
Keywords Albinism;Copper;Glycoprotein;Melanin biosynthesis;Membrane;Metal-binding;Monooxygenase;Oxidoreductase;Reference proteome;Signal;Transmembrane;Transmembrane helix
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000250|UniProtKB:P14679}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P14679}. Melanosome {ECO:0000250|UniProtKB:P11344}. Note=Proper trafficking to melanosome is regulated by SGSM2, ANKRD27, RAB9A, RAB32 and RAB38. {ECO:0000250|UniProtKB:P11344}.
Modified Residue
Post Translational Modification PTM: Glycosylated. {ECO:0000250|UniProtKB:P11344}.
Signal Peptide SIGNAL 1..17; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 60,304
Kinetics
Metal Binding METAL 180; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 202; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 211; /note=Copper A; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 363; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 367; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19; METAL 390; /note=Copper B; /evidence=ECO:0000250|UniProtKB:Q9ZP19
Rhea ID RHEA:34287; RHEA:18117
Cross Reference Brenda